Solvent perturbation and surface accessibility of the tryptophyl and tyrosyl groups in black-eyed pea trypsin and chymotrypsin inhibitor.

The solvent perturbation behavior of tyrosyl and tryptophyl residues in the black-eyed pea trypsin and chymotrypsin inhibitor have been studied using several perturbants ranging in molecular diameter from 2.8 to 9.4 A. The single tyrosyl and the single tryptophyl residues of the protein appear to be largely exposed to solvent access.